We are offering RapiData 2014, the sixteenth offering of our popular
course:
Rapid Data Collection and Structure Solving at the NSLS: A Practical
Course in Macromolecular X-Ray Diffraction Measurement
The course will be held 27 April - 2 May 2013:
http://www.bnl.gov/RapiData/.
Its possible you are in a lower space group, perhaps with some twinning, but your search
model is different enough to only find a "solution" when things are over-merged.
Try refining your P6522 model against data merged in P65. If the other copy (symmetry mate in
P6522) does not show up, you ma
We had this happen with RPA14/32 heterodimer, we kept the two peaks
separate, and then grew crystals from each but in different space groups
and diffraction resolution. See Habel, J. E., Ohren, J. F. and Borgstahl,
G. E. O. "Dynamic light scattering analysis of full-length, human RPA14/32
dimer:
I have some SIRAS data of a known structure. I want to get the
isomorphous and anomalous occupancy and phasing power from my data.
What's the best software to do this?
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All Things Serve the Beam
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It might be that the protein is innocent and the FPLC is guilty. If FPLC pump
needs maintenance and is stuttering a bit when running at high pressure, the
salt gradient won't be as smooth as you'd like. If you have an ionic strength
detector, that trace will tell you. Otherwise, see if other
Hi Acoot,
There are a lot of great suggestions here already. I've also run into this
phenomenon in couple of cases. The first was a binding protein in mixed
bound and unbound forms. The second was a case of heterogeneous
post-translational modification. In both cases I could only get crystals
fro
